Výsledky vyhledávání - "William C. Unrath"

Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin

Autor: Wanjian Tang, Jinghua Ge, William C. Unrath, Christopher M. Yengo, Rohini Desetty

Publikováno v: Biophys J

Cardiac muscle contraction is driven by the molecular motor myosin, which uses the energy from ATP hydrolysis to generate a power stroke when interacting with actin filaments, although it is unclear how this mechanism is impaired by mutations in myos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::892f06a0a71aae7a1e73927aff41fb39
https://doi.org/10.1016/j.bpj.2021.04.007

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Cardiomyopathy Mutations Impact the Power Stroke of Human Cardiac Myosin

Autor: Wanjian Tang, Rohini Desetty, Christopher M. Yengo, William C. Unrath, Jinghua Ge

Cardiac muscle contraction is driven by the molecular motor myosin that uses the energy from ATP hydrolysis to generate a power stroke when interacting with actin filaments, while it is unclear how this mechanism is impaired by mutations in myosin th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::62d07bfbaba3fb96a474cf8b0a0a28ae
https://doi.org/10.1101/2020.12.08.416511

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Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil

Autor: Christopher M. Yengo, William C. Unrath, Rohini Desetty, Wanjian Tang

Publikováno v: J Biol Chem

We investigated a dilated cardiomyopathy (DCM) mutation (F764L) in human β-cardiac myosin by determining its motor properties in the presence and absence of the heart failure drug omecamtive mecarbil (OM). The mutation is located in the converter do

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00ce32c1b7c5606532e32640257811f5
https://europepmc.org/articles/PMC6873177/

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Impact of the Motor and Tail Domains of Class III Myosins on Regulating the Formation and Elongation of Actin Protrusions

Autor: Meredith L. Weck, Manmeet H. Raval, James W. Gallagher, Christopher M. Yengo, Matthew J. Tyska, Omar A. Quintero, William C. Unrath, Runjia Cui, Bechara Kachar

Publikováno v: Journal of Biological Chemistry. 291:22781-22792

Class III myosins (MYO3A and MYO3B) are proposed to function as transporters as well as length and ultrastructure regulators within stable actin-based protrusions such as stereocilia and calycal processes. MYO3A differs from MYO3B in that it contains

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4723cb730ba6a6af7e438316e7da17f7
https://doi.org/10.1074/jbc.m116.733741

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Converter domain mutations in myosin alter structural kinetics and motor function

Autor: Joseph M. Muretta, Laura K. Gunther, Wanjian Tang, Shane D. Walton, Darshan V. Trivedi, William C. Unrath, John A. Rohde, David D. Thomas, Christopher M. Yengo

Publikováno v: The Journal of biological chemistry. 294(5)

Myosins are molecular motors that use a conserved ATPase cycle to generate force. We investigated two mutations in the converter domain of myosin V (R712G and F750L) to examine how altering specific structural transitions in the motor ATPase cycle ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a93f1ffcafc742381a4f8907e6e86759
https://pubmed.ncbi.nlm.nih.gov/30518549

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Omecamtiv Mecarbil Enhances the Duty Ratio of Human β-Cardiac Myosin Resulting in Increased Calcium Sensitivity and Slowed Force Development in Cardiac Muscle*

Autor: Michael J. Previs, Anja M. Swenson, Christopher M. Fetrow, Wanjian Tang, William C. Unrath, Cheavar A. Blair, Christopher M. Yengo, Kenneth S. Campbell

The small molecule drug omecamtiv mecarbil (OM) specifically targets cardiac muscle myosin and is known to enhance cardiac muscle performance, yet its impact on human cardiac myosin motor function is unclear. We expressed and purified human β-cardia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abfea7aa280886f169e79add066ce05f
https://europepmc.org/articles/PMC5339759/

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Biochemical and bioinformatic analysis of the myosin-XIX motor domain

Autor: William C. Unrath, Christopher M. Yengo, Rebecca C. Adikes, Omar A. Quintero

Publikováno v: Cytoskeleton. 70:281-295

Mitochondrial dynamics are dependent on both the microtubule and actin cytoskeletal systems. Evidence for the involvement of myosin motors has been described in many systems, and until recently a candidate mitochondrial transport motor had not been d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3d42eb0cee5f081c9a0a391d8299e826
https://doi.org/10.1002/cm.21110

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Myosin IIIB Uses an Actin-Binding Motif in Its Espin-1 Cargo to Reach the Tips of Actin Protrusions

Autor: Uri Manor, William C. Unrath, M'hamed Grati, Raymond C. Merritt, Felipe T. Salles, Andréa C. Dosé, Bechara Kachar, Christopher M. Yengo, Omar A. Quintero

Publikováno v: Current Biology. 22(4):320-325

SummaryMyosin IIIA (MYO3A) targets actin protrusion tips using a motility mechanism dependent on both motor and tail actin-binding activity [1]. We show that myosin IIIB (MYO3B) lacks tail actin-binding activity and is unable to target COS7 cell filo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78644d8111df9c59668bc071109fcdd7

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